DOCSLIB.ORG

Syndecan-1 (DL-101): Sc-12765

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Syndecan-1 (DL-101): Sc-12765 SANTA CRUZ BIOTECHNOLOGY, INC. Syndecan-1 (DL-101): sc-12765 BACKGROUND STORAGE Syndecan-1 (SYND1), also designated CD138, is a type I integral membrane Store at 4° C, **DO NOT FREEZE**. Stable for one year from the date of proteoglycan that contains both chondroitin sulfate and heparan sulfate shipment. Non-hazardous. No MSDS required. groups. It is expressed in mouse on pre-B cells, immature B cells and plasma cells. Syndecan-1 is also found on the basolateral surfaces of epithelial cells, DATA endothelial cells of sprouting capillaries and embryonic condensing mesen- A B chymal cells. Syndecan-1 functions as an extracellular matrix receptor which AB C DE binds to collagens, Fibronectin and Thrombospondin. It has been shown to 132 K – < co-localize with Actin-rich filaments and may act to link the cytoskeleton to Syndecan-1 90 K – the extracellular matrix. 55 K – CHROMOSOMAL LOCATION 43 K – Genetic locus: SDC1 (human) mapping to 2p24.1; Sdc1 (mouse) mapping to 12 A1.1. Syndecan-1 (DL-101): sc-12765.Western blot analysis Syndecan-1 (DL-101): sc-12765. Immunofluorescence of Syndecan-1 expressioninRaji(A), HeLa (B), MCF7 (C), staining of methanol-fixed HeLa cells showing mem- SOURCE Ramos (D)andHep G2 (E)wholecell lysates. brane staining (A). Immunoperoxidase staining of for- malin fixed, paraffin-embedded human small intestine Syndecan-1 (DL-101) is a mouse monoclonal antibody raised against tissue showing membrane and cytoplasmic staining of glandular cells (B). Syndecan-1 of human origin. SELECT PRODUCT CITATIONS PRODUCT 1. Slimani, H., et al. 2003. Interaction of RANTES with Syndecan-1 and Each vial contains 200 µg IgG kappa light chain in 1.0 ml of PBS with < 0.1% 1 Syndecan-4 expressed by human primary macrophages. Biochim. Biophys. sodium azide and 0.1% gelatin. Acta 1617: 80-88. Syndecan-1 (DL-101) is available conjugated to agarose (sc-12765 AC), 2. Shi, Q., et al. 2013. Syndecan-1 serves as the major receptor for attach- 500 µg/0.25 ml agarose in 1 ml, for IP; to HRP (sc-12765 HRP), 200 µg/ml, ment of hepatitis C virus to the surfaces of hepatocytes. J. Virol. 87: for WB, IHC(P) and ELISA; to either phycoerythrin (sc-12765 PE), fluorescein 6866-6875. (sc-12765 FITC), Alexa Fluor® 488 (sc-12765 AF488), Alexa Fluor® 546 (sc-12765 AF546), Alexa Fluor® 594 (sc-12765 AF594) or Alexa Fluor® 647 3. dela Paz, N.G., et al. 2014. Heparan sulfates mediate the interaction (sc-12765 AF647), 200 µg/ml, for WB (RGB), IF, IHC(P) and FCM; and to either between platelet endothelial cell adhesion molecule-1 (PECAM-1) and Alexa Fluor® 680 (sc-12765 AF680) or Alexa Fluor® 790 (sc-12765 AF790), the Gα q/11 subunits of heterotrimeric G proteins. J. Biol. Chem. 289: 200 µg/ml, for Near-Infrared (NIR) WB, IF and FCM. 7413-7424. Alexa Fluor® is a trademark of Molecular Probes, Inc., Oregon, USA 4. Zaragosi, L.E., et al. 2015. Syndecan-1 regulates adipogenesis: new insights in dedifferentiated liposarcoma tumorigenesis. Carcinogenesis APPLICATIONS 36: 32-40. Syndecan-1 (DL-101) is recommended for detection of the ectodomain of 5. Bengtsson, E., et al. 2016. The leucine-rich repeat protein PRELP binds Syndecan-1 of mouse, rat and human origin by Western Blotting (starting fibroblast cell-surface proteoglycans and enhances focal adhesion for- dilution 1:200, dilution range 1:100-1:1000), immunoprecipitation [1-2 µg mation. Biochem. J. 473: 1153-1164. per 100-500 µg of total protein (1 ml of cell lysate)], immunofluorescence 6. Urbinati, C., et al. 2017. Syndecan-1 increases B-lymphoid cell extrava- (starting dilution 1:50, dilution range 1:50-1:500), immunohistochemistry sation in response to HIV-1 Tat via α β /pp60src/pp125FAK pathway. (including paraffin-embedded sections) (starting dilution 1:50, dilution v 3 Oncogene 36: 2609-2618. range 1:50-1:500) and flow cytometry (1 µg per 1 x 106 cells). 7. Niu, T., et al. 2019. Endomucin restores depleted endothelial glycocalyx Suitable for use as control antibody for Syndecan-1 siRNA (h): sc-36587, in the retinas of streptozotocin-induced diabetic rats. FASEB J. 33: Syndecan-1 siRNA (m): sc-36586, Syndecan-1 shRNA Plasmid (h): 13346-13357. sc-36587-SH, Syndecan-1 shRNA Plasmid (m): sc-36586-SH, Syndecan-1 shRNA (h) Lentiviral Particles: sc-36587-V and Syndecan-1 shRNA (m) 8. Gkogkou, P., et al. 2020. E-cadherin and Syndecan-1 expression in patients Lentiviral Particles: sc-36586-V. with advanced non-small cell lung cancer treated with chemoradiotherapy. In Vivo 34: 453-459. Molecular Weight of Syndecan-1: 85 kDa. Positive Controls: Raji whole cell lysate: sc-364236, HeLa whole cell lysate: RESEARCH USE sc-2200 or MCF7 whole cell lysate: sc-2206. For research use only, not for use in diagnostic procedures. Santa Cruz Biotechnology, Inc. 1.800.457.3801 831.457.3800 fax 831.457.3801 Europe +00800 4573 8000 49 6221 4503 0 www.scbt.com.
Load more

Recommended publications
  • Distribution and Clinical Significance of Heparan Sulfate Proteoglycans in Ovarian Cancer
    5178 Vol. 10, 5178–5186, August 1, 2004 Clinical Cancer Research Distribution and Clinical Significance of Heparan Sulfate Proteoglycans in Ovarian Cancer E. June Davies,1 Fiona H. Blackhall,1 decan-1 and glypican-1 were poor prognostic factors for Jonathan H. Shanks,2 Guido David,3 survival in univariate analysis. Alan T. McGown,4 Ric Swindell,5 Conclusion: We report for the first time distinct pat- 6 7 terns of expression of cell surface and extracellular matrix Richard J. Slade, Pierre Martin-Hirsch, heparan sulfate proteoglycans in normal ovary compared 1 1 John T. Gallagher, and Gordon C. Jayson with ovarian tumors. These data reinforce the role of the 1Cancer Research UK and University of Manchester Department of tumor stroma in ovarian adenocarcinoma and suggest that Medical Oncology, Paterson Institute for Cancer Research, stromal induction of syndecan-1 contributes to the patho- Manchester, England; 2Department of Histopathology, Christie Hospital NHS Trust, Manchester, England; 3Department of Medicine, genesis of this malignancy. University of Leuven, Leuven, Belgium.; 4Cancer Research UK Department of Experimental Pharmacology, Paterson Institute for Cancer Research, Manchester, England; 5Department of Medical INTRODUCTION Statistics, Christie Hospital NHS Trust, Manchester, England; The heparan sulfate proteoglycans (HSPGs) play diverse 6Department of Obstetrics and Gynaecology, Hope Hospital, Salford, Manchester, England; 7Department of Gynaecological Oncology, St. roles in tumor biology by mediating adhesion and migration
    [Show full text]
  • And MMP-Mediated Cell–Matrix Interactions in the Tumor Microenvironment
    International Journal of Molecular Sciences Review Hold on or Cut? Integrin- and MMP-Mediated Cell–Matrix Interactions in the Tumor Microenvironment Stephan Niland and Johannes A. Eble * Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, 48149 Münster, Germany; [email protected] * Correspondence: [email protected] Abstract: The tumor microenvironment (TME) has become the focus of interest in cancer research and treatment. It includes the extracellular matrix (ECM) and ECM-modifying enzymes that are secreted by cancer and neighboring cells. The ECM serves both to anchor the tumor cells embedded in it and as a means of communication between the various cellular and non-cellular components of the TME. The cells of the TME modify their surrounding cancer-characteristic ECM. This in turn provides feedback to them via cellular receptors, thereby regulating, together with cytokines and exosomes, differentiation processes as well as tumor progression and spread. Matrix remodeling is accomplished by altering the repertoire of ECM components and by biophysical changes in stiffness and tension caused by ECM-crosslinking and ECM-degrading enzymes, in particular matrix metalloproteinases (MMPs). These can degrade ECM barriers or, by partial proteolysis, release soluble ECM fragments called matrikines, which influence cells inside and outside the TME. This review examines the changes in the ECM of the TME and the interaction between cells and the ECM, with a particular focus on MMPs. Keywords: tumor microenvironment; extracellular matrix; integrins; matrix metalloproteinases; matrikines Citation: Niland, S.; Eble, J.A. Hold on or Cut? Integrin- and MMP-Mediated Cell–Matrix 1. Introduction Interactions in the Tumor Microenvironment.
    [Show full text]
  • Biosynthesized Multivalent Lacritin Peptides Stimulate Exosome Production in Human Corneal Epithelium
    International Journal of Molecular Sciences Article Biosynthesized Multivalent Lacritin Peptides Stimulate Exosome Production in Human Corneal Epithelium Changrim Lee 1, Maria C. Edman 2 , Gordon W. Laurie 3 , Sarah F. Hamm-Alvarez 1,2,* and J. Andrew MacKay 1,2,4,* 1 Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, CA 90033, USA; [email protected] 2 Department of Ophthalmology, USC Roski Eye Institute and Keck School of Medicine, University of Southern California, Los Angeles, CA 90033, USA; [email protected] 3 Department of Cell Biology, School of Medicine, University of Virginia, Charlottesville, VA 22908, USA; [email protected] 4 Department of Biomedical Engineering, Viterbi School of Engineering, University of Southern California, Los Angeles, CA 90089, USA * Correspondence: [email protected] (S.F.H.-A.); [email protected] (J.A.M.) Received: 30 July 2020; Accepted: 24 August 2020; Published: 26 August 2020 Abstract: Lacripep is a therapeutic peptide derived from the human tear protein, Lacritin. Lacripep interacts with syndecan-1 and induces mitogenesis upon the removal of heparan sulfates (HS) that are attached at the extracellular domain of syndecan-1. The presence of HS is a prerequisite for the syndecan-1 clustering that stimulates exosome biogenesis and release. Therefore, syndecan-1- mediated mitogenesis versus HS-mediated exosome biogenesis are assumed to be mutually exclusive. This study introduces a biosynthesized fusion between Lacripep and an elastin-like polypeptide named LP-A96, and evaluates its activity on cell motility enhancement versus exosome biogenesis. LP-A96 activates both downstream pathways in a dose-dependent manner.
    [Show full text]
  • Analysis of Transport and Targeting of Syndecan-1: Effect of Cytoplasmic Tail Deletions Heini M
    Molecular Biology of the Cell Vol. 5, 1325-1339, December 1994 Analysis of Transport and Targeting of Syndecan-1: Effect of Cytoplasmic Tail Deletions Heini M. Miettinen,*t# Susan N. Edwards,* and Markku Jalkanen* *Centre for Biotechnology, FIN-20521 Turku, Finland; and tDepartment of Medical Biochemistry, University of Turku, FIN-20520 Turku, Finland Submitted October 6, 1994; Accepted October 26, 1994 Monitoring Editor: Richard Hynes Madin-Darby canine kidney (MDCK) cells and Chinese hamster ovary (CHO) cells were transfected with wild-type and cytoplasmic deletion mutants of mouse syndecan-1 to study the requirements for transport and polarized expression of this proteoglycan. Expression in MDCK cells revealed that wild-type syndecan-1 is directed to the basolateral surface via a brefeldin A-insensitive route. A deletion of the last 12 amino acids of the syndecan- 1 cytoplasmic tail (CT22) was sufficient to result in the appearance of mutant proteoglycans at both the basolateral and apical cell surfaces. Treatment with brefeldin A was able to prevent apical transport of the mutants. We thus propose that the C-terminal part of the cytoplasmic tail is required for steady-state basolateral distribution of syndecan-1. In CHO cells a deletion of the last 25 or 33 amino acids of the 34-residue cytoplasmic domain (CT9 and CT1, respectively) resulted in partial retention of the mutants in the endoplasmic reticulum (ER). A deletion mutant lacking the last 12 amino acids (CT22) was not retained. Interestingly, the unglycosylated core proteins of the CT9 and CT1 mutants showed a significantly lower apparent molecular weight when analyzed by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis than wild-type syndecan- 1.
    [Show full text]
  • The Adhesion G Protein-Coupled Receptor GPR56 Is a Cell-Autonomous Regulator of Oligodendrocyte Development
    ARTICLE Received 27 May 2014 | Accepted 14 Dec 2014 | Published 21 Jan 2015 DOI: 10.1038/ncomms7121 OPEN The adhesion G protein-coupled receptor GPR56 is a cell-autonomous regulator of oligodendrocyte development Stefanie Giera1,*, Yiyu Deng1,*,w, Rong Luo1,*, Sarah D. Ackerman2, Amit Mogha2, Kelly R. Monk2,3, Yanqin Ying1, Sung-Jin Jeong1,w, Manabu Makinodan4,5, Allison R. Bialas4,5, Bernard S. Chang6, Beth Stevens4,5, Gabriel Corfas4,5,w & Xianhua Piao1 Mutations in GPR56, a member of the adhesion G protein-coupled receptor family, cause a human brain malformation called bilateral frontoparietal polymicrogyria (BFPP). Magnetic resonance imaging (MRI) of BFPP brains reveals myelination defects in addition to brain malformation. However, the cellular role of GPR56 in oligodendrocyte development remains unknown. Here, we demonstrate that loss of Gpr56 leads to hypomyelination of the central nervous system in mice. GPR56 levels are abundant throughout early stages of oligodendrocyte development, but are downregulated in myelinating oligodendrocytes. Gpr56-knockout mice manifest with decreased oligodendrocyte precursor cell (OPC) proliferation and diminished levels of active RhoA, leading to fewer mature oligodendrocytes and a reduced number of myelinated axons in the corpus callosum and optic nerves. Conditional ablation of Gpr56 in OPCs leads to a reduced number of mature oligodendrocytes as seen in constitutive knockout of Gpr56. Together, our data define GPR56 as a cell-autonomous regulator of oligodendrocyte development. 1 Division of Newborn Medicine, Department of Medicine, Boston Children’s Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA. 2 Department of Developmental Biology, Washington University School of Medicine, St Louis, Missouri 63110, USA.
    [Show full text]
  • Heparan Sulfate Proteoglycans Present PCSK9 to the LDL Receptor
    ARTICLE DOI: 10.1038/s41467-017-00568-7 OPEN Heparan sulfate proteoglycans present PCSK9 to the LDL receptor Camilla Gustafsen 1, Ditte Olsen1, Joachim Vilstrup 2, Signe Lund1, Anika Reinhardt3, Niels Wellner1, Torben Larsen4, Christian B.F. Andersen1, Kathrin Weyer1, Jin-ping Li5, Peter H. Seeberger6, Søren Thirup 2, Peder Madsen1 & Simon Glerup1 Coronary artery disease is the main cause of death worldwide and accelerated by increased plasma levels of cholesterol-rich low-density lipoprotein particles (LDL). Circulating PCSK9 contributes to coronary artery disease by inducing lysosomal degradation of the LDL receptor (LDLR) in the liver and thereby reducing LDL clearance. Here, we show that liver heparan sulfate proteoglycans are PCSK9 receptors and essential for PCSK9-induced LDLR degra- dation. The heparan sulfate-binding site is located in the PCSK9 prodomain and formed by surface-exposed basic residues interacting with trisulfated heparan sulfate disaccharide repeats. Accordingly, heparan sulfate mimetics and monoclonal antibodies directed against the heparan sulfate-binding site are potent PCSK9 inhibitors. We propose that heparan sulfate proteoglycans lining the hepatocyte surface capture PCSK9 and facilitates subsequent PCSK9:LDLR complex formation. Our findings provide new insights into LDL biology and show that targeting PCSK9 using heparan sulfate mimetics is a potential therapeutic strategy in coronary artery disease. 1 Department of Biomedicine, Aarhus University, Ole Worms Allé 3, 8000 Aarhus, Denmark. 2 Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10, 8000 Aarhus, Denmark. 3 Scienion AG, Volmerstrasse 7b, 12489 Berlin, Germany. 4 Department of Animal Science, Aarhus University, Blichers Allé 20, 8830 Tjele, Denmark. 5 Department of Medical Biochemistry and Microbiology, University of Uppsala, Husarg.
    [Show full text]
  • Title: the Heparan Sulfate Proteoglycan Syndecan-1 Influences Local Bone Cell
    bioRxiv preprint doi: https://doi.org/10.1101/852590; this version posted November 2, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. Title: The heparan sulfate proteoglycan Syndecan-1 influences local bone cell communication via the RANKL/OPG axis Short title: Syndecan-1 in local bone cell communication Melanie Timmen*1, Heriburg Hidding1, Martin Götte2, Thaqif El Khassawna3, Daniel Kronenberg1 and Richard Stange1 Dr. rer. nat. Melanie Timmen (corresponding author) 1Department of Regenerative Musculoskeletal Medicine, Institute of Musculoskeletal Medicine, University Muenster, Germany; [email protected] Dr. rer. nat. Heriburg Hidding, 1Department of Regenerative Musculoskeletal Medicine, Institute of Musculoskeletal Medicine, University Muenster, Germany [email protected] Prof. Dr. rer. nat. Martin Götte; 2Department of Gynecology and Obstetrics, University Hospital Muenster, Germany [email protected] Dr. rer. nat. Thaqif El Khassawna; 3Experimental Trauma Surgery, Justus-Liebig University Giessen, Germany [email protected] Dr. rer. nat. Daniel Kronenberg; 1Department of Regenerative Musculoskeletal Medicine, Institute of Musculoskeletal Medicine, University Muenster, Germany [email protected] Prof. Dr. med Richard Stange; 1Department of Regenerative Musculoskeletal Medicine, Institute of Musculoskeletal Medicine, University Muenster, Germany [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/852590; this version posted November 2, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.
    [Show full text]
  • Immunodiagnostic Analysis of Lacritin in Human Breast Milk Veronica Christine Vassilev James Madison University
    James Madison University JMU Scholarly Commons Senior Honors Projects, 2010-current Honors College Spring 2014 Immunodiagnostic analysis of lacritin in human breast milk Veronica Christine Vassilev James Madison University Follow this and additional works at: https://commons.lib.jmu.edu/honors201019 Recommended Citation Vassilev, Veronica Christine, "Immunodiagnostic analysis of lacritin in human breast milk" (2014). Senior Honors Projects, 2010-current. 492. https://commons.lib.jmu.edu/honors201019/492 This Thesis is brought to you for free and open access by the Honors College at JMU Scholarly Commons. It has been accepted for inclusion in Senior Honors Projects, 2010-current by an authorized administrator of JMU Scholarly Commons. For more information, please contact [email protected]. Immunodiagnostic Analysis of Lacritin in Human Breast Milk _______________________ A Project Presented to the Faculty of the Undergraduate Colleges of Integrated Science and Engineering & Science and Mathematics James Madison University _______________________ in Partial Fulfillment of the Requirements for the Degree of Bachelor of Science _______________________ by Veronica Christine Vassilev May 2014 Accepted by the faculty of the Departments of Integrated Science and Technology & Biology, James Madison University, in partial fulfillment of the requirements for the Degree of Bachelor of Science. FACULTY COMMITTEE: HONORS PROGRAM APPROVAL: Project Advisor: Robert L. McKown, Ph.D., Barry Falk, Ph.D., Professor, ISAT Director, Honors Program Reader: Kyle Seifert, Ph.D., Associate Professor, Biology Reader: Ron Raab, Ph.D., Professor, ISAT Table of Contents List of Figures 3 Acknowledgements 4 Abstract 5 Introduction 6 Materials and Methods 11 Results 14 Discussion 21 References 26 2 List of Figures Figures Figure 1.
    [Show full text]
  • Tyrosine 51 Residue of the Syndecan-2 Extracellular Domain Is Involved in the Interaction with and Activation of Pro-Matrix Meta
    www.nature.com/scientificreports OPEN Tyrosine 51 residue of the syndecan-2 extracellular domain is involved in the interaction Received: 14 January 2019 Accepted: 11 July 2019 with and activation of pro-matrix Published: xx xx xxxx metalloproteinase-7 Bohee Jang1, Ji-Hye Yun2, Sojoong Choi1, Jimin Park3, Dong Hae Shin3, Seung-Taek Lee 2, Weontae Lee2 & Eok-Soo Oh1 Although syndecan-2 is known to interact with the matrix metalloproteinase-7 (MMP-7), the details of their interaction were unknown. Our experiments with a series of syndecan-2 extracellular domain deletion mutants show that the interaction is mediated through an interaction of the extracellular domain of syndecan-2 (residues 41 to 60) with the α2 helix-loop-α3 helix in the pro-domain of MMP-7. NMR and molecular docking model show that Glu7 of the α1 helix, Glu32 of the α2 helix, and Gly48 and Ser52 of the α2 helix-loop-α3 helix of the MMP-7 pro-domain form the syndecan-2-binding pocket, which is occupied by the side chain of tyrosine residue 51 (Tyr51) of syndecan-2. Consistent with this notion, the expression of a syndecan-2 mutant in which Tyr51 was changed to Ala diminished the interaction between the syndecan-2 extracellular domain and the pro-domain of MMP-7. Furthermore, HT-29 colon adenocarcinoma cells expressing the interaction-defective mutant exhibited reductions in the cell-surface localization of MMP-7, the processing of pro-MMP-7 into active MMP-7, the MMP-7- mediated extracellular domain shedding of both syndecan-2 and E-cadherin, and syndecan-2-mediated anchorage-independent growth.
    [Show full text]
  • The Expression of Cell Surface Heparan Sulfate Proteoglycans and Their Roles in Turkey Skeletal Muscle Formation
    THE EXPRESSION OF CELL SURFACE HEPARAN SULFATE PROTEOGLYCANS AND THEIR ROLES IN TURKEY SKELETAL MUSCLE FORMATION DISSERTATION Presented in Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy in the Graduate School of The Ohio State University By Xiaosong Liu, M.S. ***** The Ohio State University 2003 Dissertation Committee: Approved by Dr. Sandra G. Velleman, Advisor Dr. Karl E. Nestor Dr. Joy L. Pate _______________________ Advisor Dr. Wayne L. Bacon Department of Animal Sciences ABSTRACT Skeletal muscle myogenesis is a series of highly organized processes including cell migration, adhesion, proliferation, and differentiation that are precisely regulated by the extrinsic environment of muscle cells. Fibroblast growth factor 2 (FGF2) is one of the key growth factors involved in the regulation of skeletal muscle myogenesis. Since FGF2 is a potent stimulator of skeletal muscle cell proliferation but an intense inhibitor of cell differentiation, changes in FGF2 signaling to muscle cells will influence cell behavior and result in differences in cell proliferation and differentiation. As the cell surface heparan sulfate proteoglycans (HSPG), syndecans and glypicans, are the low- affinity receptors of FGF2 and function to regulate the binding of FGF2 to the high- affinity fibroblast growth factor receptors (FGFR) and affect the activity of FGF2, differences in the expression of these molecules may cause alterations in cell responsiveness to FGF2 stimulation, which can lead to changes in skeletal muscle development and growth. However, the precise functional differences of syndecans and glypicans in FGF2 signaling are unknown to date. Our hypothesis is that syndecans and glypicans may play different roles in regulating the FGF2-FGFR interaction, and the relative expression of these molecules is critical for determining the cell status in proliferation and differentiation.
    [Show full text]
  • Syndecan-4 Core Protein and Focal Adhesions 3435 Represent Typical Staining Patterns Observed at the Indicated Time Points
    Journal of Cell Science 112, 3433-3441 (1999) 3433 Printed in Great Britain © The Company of Biologists Limited 1999 JCS4670 Syndecan-4 core protein is sufficient for the assembly of focal adhesions and actin stress fibers Frank Echtermeyer, Peter C. Baciu*, Stefania Saoncella, Yimin Ge and Paul F. Goetinck‡ Cutaneous Biology Research Center, Massachusetts General Hospital, Harvard Medical School, Building 149, 13th Street, Charlestown, Massachusetts 02129, USA *Present address: Allergan Inc., 2525 Dupont Drive, Irvine, CA 92612, USA ‡Author for correspondence (e-mail: [email protected]) Accepted 20 April; published on WWW 30 September 1999 SUMMARY The formation of focal adhesions and actin stress fibers on syndecan-4 core protein in these mutant cells increases cell fibronectin is dependent on signaling through β1 integrins spreading and is sufficient for these cells to assemble actin and the heparan sulfate proteoglycan syndecan-4, and we stress fibers and focal adhesions similar to wild-type cells have analyzed the requirement of the glycosaminoglycan seeded on fibronectin and vitronectin matrices. Syndecan- chains of syndecan-4 during these events. Chinese hamster 4 core protein colocalizes to focal contacts in mutant cells ovary cells with mutations in key enzymes of the that have been transfected with the syndecan-4 core protein glycanation process do not synthesize glycosaminoglycan cDNA. These data indicate an essential role for the core chains and are unable to assemble actin stress fibers and protein of syndecan-4 in the generation of signals leading focal contacts when cultured on fibronectin. Transfection to actin stress fiber and focal contact assembly. of the mutant cells with a cDNA that encodes the core protein of chicken syndecan-4 leads to the production Key words: Syndecan, Heparan sulfate proteoglycan, Cell of unglycanated core protein.
    [Show full text]
  • The Role of Syndecan-1 in Cellular Signaling and Its Effects on Heparan
    REVIEW ARTICLE published: 19 December 2013 doi: 10.3389/fonc.2013.00310 The role of syndecan-1 in cellular signaling and its effects on heparan sulfate biosynthesis in mesenchymal tumors Tünde Szatmári and Katalin Dobra* Department of Laboratory Medicine, Karolinska Institutet, Karolinska University Hospital, Stockholm, Sweden Edited by: Proteoglycans (PGs) and in particular the syndecans are involved in the differentiation Elvira V. Grigorieva, Institute of process across the epithelial-mesenchymal axis, principally through their ability to bind Molecular Biology and Biophysics SB growth factors and modulate their downstream signaling. Malignant tumors have indi- RAMS, Russia Reviewed by: vidual proteoglycan profiles, which are closely associated with their differentiation and Markus A. N. Hartl, University of biological behavior, mesenchymal tumors showing a different profile from that of epithelial Innsbruck, Austria tumors. Syndecan-1 is the main syndecan of epithelial malignancies, whereas in sarcomas Swapna Asuthkar, University of Illinois its expression level is generally low, in accordance with their mesenchymal phenotype and College of Medicine at Peoria, USA highly malignant behavior. This proteoglycan is often overexpressed in adenocarcinoma *Correspondence: Katalin Dobra, Department of cells, whereas mesothelioma and fibrosarcoma cells express syndecan-2 and syndecan-4 Laboratory Medicine, Karolinska more abundantly. Increased expression of syndecan-1 in mesenchymal tumors changes Institutet, Karolinska University the tumor cell morphology to an epithelioid direction whereas downregulation results in Hospital F-46, SE-141 86 Stockholm, a change in shape from polygonal to spindle-like morphology. Although syndecan-1 plays Sweden e-mail: [email protected] major roles on the cell-surface, there are also intracellular functions, which are not very well studied.
    [Show full text]